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NUBP1_CAEEL
ID   NUBP1_CAEEL             Reviewed;         313 AA.
AC   Q93459;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 homolog {ECO:0000255|HAMAP-Rule:MF_03038};
DE   AltName: Full=Nucleotide binding protein 1 homolog {ECO:0000312|WormBase:F10G8.6};
GN   Name=nubp-1 {ECO:0000312|WormBase:F10G8.6};
GN   ORFNames=F10G8.6 {ECO:0000312|WormBase:F10G8.6};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA   Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA   Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA   Santama N.;
RT   "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT   ciliogenesis.";
RL   Cell. Mol. Life Sci. 71:517-538(2014).
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC       assembly (CIA) machinery. Required for maturation of extramitochondrial
CC       Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold
CC       complex, mediating the de novo assembly of an Fe-S cluster and its
CC       transfer to target apoproteins (By similarity). Regulates cilium
CC       formation and structure (PubMed:23807208). {ECO:0000255|HAMAP-
CC       Rule:MF_03038, ECO:0000269|PubMed:23807208}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03038};
CC       Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable
CC       clusters in the N-termini of NUBP1 and two labile, bridging clusters
CC       between subunits of the NUBP1-NUBP2 heterotetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_03038};
CC   -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains.
CC       {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}. Cell
CC       projection {ECO:0000269|PubMed:23807208}.
CC   -!- TISSUE SPECIFICITY: Expressed in head amphid and labial ciliated
CC       sensory neurons and tail phasmid ciliated chemosensory neurons.
CC       {ECO:0000269|PubMed:23807208}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in abnormal cilia
CC       morphology with the formation of 'wing-shaped' cilia structures and
CC       additional dendritic ciliated endings in amphid wing B (AWB) olfactory
CC       amphid neurons. {ECO:0000269|PubMed:23807208}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
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DR   EMBL; Z80216; CAB02285.2; -; Genomic_DNA.
DR   PIR; T20728; T20728.
DR   RefSeq; NP_492653.2; NM_060252.4.
DR   AlphaFoldDB; Q93459; -.
DR   SMR; Q93459; -.
DR   BioGRID; 38289; 3.
DR   IntAct; Q93459; 1.
DR   STRING; 6239.F10G8.6; -.
DR   iPTMnet; Q93459; -.
DR   EPD; Q93459; -.
DR   PaxDb; Q93459; -.
DR   PeptideAtlas; Q93459; -.
DR   EnsemblMetazoa; F10G8.6.1; F10G8.6.1; WBGene00008664.
DR   GeneID; 172868; -.
DR   KEGG; cel:CELE_F10G8.6; -.
DR   UCSC; F10G8.6; c. elegans.
DR   CTD; 172868; -.
DR   WormBase; F10G8.6; CE30749; WBGene00008664; nubp-1.
DR   eggNOG; KOG3022; Eukaryota.
DR   GeneTree; ENSGT00950000183193; -.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   InParanoid; Q93459; -.
DR   OMA; QHITFKD; -.
DR   OrthoDB; 1166096at2759; -.
DR   PhylomeDB; Q93459; -.
DR   PRO; PR:Q93459; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00008664; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR   GO; GO:1902855; P:regulation of non-motile cilium assembly; IMP:WormBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   HAMAP; MF_03038; NUBP1; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR028601; NUBP1/Nbp35.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR23264; PTHR23264; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; ATP-binding; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..313
FT                   /note="Cytosolic Fe-S cluster assembly factor NUBP1
FT                   homolog"
FT                   /id="PRO_0000184949"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         29
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         35
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         240
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         243
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
SQ   SEQUENCE   313 AA;  33038 MW;  471C5D7409D6661F CRC64;
     MSDVPDDANA GCPGTGSAGA GKASGCAGCP NQGSCATGQG PPPDADVPKI QDRFSRIKHK
     ILILSGKGGV GKSTLTSNLA RALASDPSKQ VAILDVDICG PSQPRMMGVE DEEVHNSADG
     WTPVGIQPNL TLMSIAFLLG DKNDAVIWRG ARKNGMIKQF LKDVDWGEVD YLLIDTPPGT
     SDEHISLVQF LLQAGPLDGA LIVSTPQEVS LLDVRKEVSF CVKTKVPILG VVENMARFVC
     PNCAHTTLLF PTSTGGAEQM CKDSNLELLA QLPLEPALAK ALDNGEDFFE TNPDSTLAKS
     FLDLAEKVKA KLV
 
 
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